Alkaline Phosphomonoesterase Activity Research Articles

Comparative study of the development of alkaline phosphodiesterase I and alkaline phosphatase in mucosa of rat jejunum and ileum.

During the early postnatal period phosphodiesterase I is almost equally distributed in the jejunum and the ileum of rat intestine. By the end of the third week after birth the specific activity in the jejunum decreases to about one-half and in the ileum to about one-tenth of the activities found on the ninth day, forming a proximo–distal gradient typical of adult animals. The activity of alkaline phosphomonoesterase in newborns is much lower than that of phosphodiesterase I and increases rapidly the first day. During the second week the specific activity of alkaline phosphatase in the ileum rises to more than double that in the jejunum and the final proximo–distal gradient is established somewhat later. For both enzymes the amount of activity appearing as soluble cytoplasmic material is highest in newborn rats and diminishes as the animals mature. The extractibility of activity from the insoluble microsomal fractions with Triton X-100 follows the same trend. After extraction of the enzymes from microsomes by treatment with tert-amyl alcohol, Triton X-100, or glycerol, most of the phosphodiesterase I activity appears in large complexes of molecular weight of several millions, but after autolysis the complexes break down to molecules of molecular weight close to 150 000 without appreciable loss of activity.

Biochemical data on some organs from normal or prolactin-treated Xenopus laevis (Daudin) adults reared in fresh and in salt water

The effects of salinity and of prolactin treatment on urea synthesis in the liver, and on the shift from ammonotelic to ureotelic excretion, were studied in adult Xenopus laevis. The activity of both arginase and urea synthesis in the liver increased in the animals reared in salt water. This rise is reduced by prolactin treatment. In addition, estimation of the activity of alkaline phosphomonoesterase (taken as a test of the functional condition of the adrenal glands) showed that it decreases in salt water animals. This decrease was more pronounced after prolactin treatment. Increase in the level of sodium in the muscle tissue, which is connected with the level of this ion in the blood, occurred in the salt water animals and was further enhanced by prolactin treatment.

Enzymatic-histochemical studies in experimental uraemia.

Permeability of the cerebral capillaries, transcellular transport of fluids, glucose and ions depend on the condition of the cell membrane. Enzymes which catalyse the energy-releasing processes are important factors in this respect. In uraemia, of ATP-ase, alkaline phosphomonoesterase activity was significantly diminished in the basement membrane of the capillaries and in the cell membranes of the pericapillary glial processes. Decreased activity of these enzymes in uraemia may increase cerebral capillary permeability, the initial phenomenon of uraemic neuropathological alterations. Disturbance in cell membrane transport in uraemia is further revealed by the pericapillary increase in the activity of alpha glycerophosphate dehydrogenase. Hypernatraemia and hyperkalaemia are supposed to promote this phenomenon. The present investigations have shown that the development of uraemia is accompanied in the cerebellum by decreased activity of succinic dehydrogenase and (to a lesser extent) alpha glycerophosphate dehydrogenase, and a considerably increased activity of lactic dehydrogenase. Anaerobic instead of oxidative glycolysis seems to get the upper hand in the energy-releasing metabolic processes of the nerve tissues in uraemia.

Inorganic pyrophosphate concentrations in the synovial fluid of arthritic patients.

Abstract A radioisotope dilution technique for measurement of inorganic pyrophosphate (PPi) in synovial fluid is described. Its precision based on duplicate measurements is ±4 μg per 100 ml. PPi levels in 20 of 23 joint fluids from patients with arthritis other than pseudogout clustered about a mean ± S.D. of 22 ± 6.3; 3 control fluids showed elevated values. Of 18 joint fluids from patients with calcium pyrophosphate crystal deposition disease (pseudogout), 15 showed inorganic PPi levels that were greater than 2 S.D. from the control mean, 2 were borderline, and one fell in the normal range. The mean ± S.D. of the group was 100.4 ± 93. Inorganic orthophosphate, total and ionized calcium, alkaline phosphomonoesterase activity against both p-nitrophenylphosphate and β-glycerophosphate, and alkaline phosphomonoesterase isozymes were not significantly different in joint fluids from control and pseudogout patients. Preliminary studies on the solubility of calcium pyrophosphate dihydrate miscocrystals in various solvents such as distilled water, Tris buffer, dialyzed and anaerobically processed fresh joint fluid and plasma are presented. The levels of PPi attained were of the same order of magnitude as those found in joint fluids from pseudogout patients. Magnesium ions and protein increased solubility; calcium and orthophosphate ions decreased it. Whether or not the PPi levels found in pseudogout fluid represent saturation levels in vivo cannot be answered from the present data.

Über die phosphatasen des menschlichen samens

In the seminal plasma of 193 human subjects acid phosphomonoesterase, and of 95 subjects alkaline phosphomonoesterase activity was measured. Thereby for the acid esterase values between 0.01 and 5.38 mMU/g protein and for the alkaline enzyme between and 3.99 mMU/g protein were obtained. These values were related to 12 different clinical and biochemical parameters of the corresponding semen. Some correlations were verified statistically.

The effect of certain cations and anions on the alkaline phosphomonoesterase activities in human dental plaque.

The effect of certain cations and anions on the alkaline phosphomonoesterase activities in human dental plaque.

Effect of age on alkaline phosphomonoesterase activity in the adrenals of male mice.

AbstractThis investigation was undertaken to examine the effects of aging on alkaline phosphomonoesterase (Alk Pase) activity in the adrenals of a highly inbred strain of C57BL/10 male mice. A total of 140 male mice were assigned to seven main groups and sacrificed at 1, 4, 8, 12, 16, 20 and 24 months of age for biochemical and morphologic evaluations of adrenal Alk Pase activity. The biochemical findings indicated that while aging may result in a decrease of serum and liver Alk Pase activity, enzyme activity in the adrenals of male mice increases to a maximum level at approximately eight months of age and subsequently decreases at each successive age level. The histochemical findings revealed that the highest concentrations of enzyme activity occurred in the fascicular and reticular zones of sexually mature male mice. There were no major variations in zonal distribution with advancing age. Electron microscopy showed Alk Pase activity along membranes of cortical cells and within the subendothelial space.The progressive increase in Alk Pase enzyme activity up to eight months of age, and the subsequent fall in activity during senescence as well as its absence in the adrenals of female mice provides further support for a role of androgen in mobilizing cortical alkaline phosphomonoesterase activity.

Alterations of alkaline phosphatase in mouse tissues after experimental infection.

SummaryThe alkaline phosphomonoes-terase activity of several mouse tissues and serum has been investigated in uninfected controls and animals infected with Diplo-coccus pneumoniae. No significant change of enzymatic activity was found in kidney, lung, sternum, femur, and spleen. As the infection progressed a decrease in activity was observed in the liver enzyme, while a marked increase occurred in small intestine. The enzymatic activity of the serum also increased during infection, but less strikingly. In organ-specific inhibition experiments it was shown that serum and intestinal enzyme behaved identically. The data support the concept that a major portion of serum AP may originate in the small intestine. Neither the infection-related increase in intestinal AP nor the fall in hepatic AP was dependent upon an intact adrenal gland in the presence of circulating glucocorticoid hormones.

Studies on American Paragonimiasis. III. Phosphomonoesterase Activity

Acid and alkaline phosphomonoesterase activity has been studied in Paragonimus kellicotti Ward, 1908. The enzymes have been partially purified by differential centrifugation and column chromatography on P-60 polyacrylamide gel. These steps also removed endogenous inorganic phosphate which allowed subsequent reactions to be completed at zero-order kinetics. The partially purified enzymes exhibited maximal activity at pH 4.5 and 9.0 against a variety of substrates. In addition, three other substrates were hydrolyzed at a maximal rate at other pH values. These included glucose6-phosphate at 6.8, AMP at 7.2, and fructose-1, 6-diphosphate at 10.0. These data indicate that a complex group of enzymes are involved in the breakdown of phosphomonoesterases by Paragonimus kellicotti. The enzymes acid phosphatase and alkaline phosphatase are known to attack a variety of both natural and synthetic substrates. They have been extensively investigated over the past decades, and have been found to occur in a number of living organisms (Schmidt, 1961; Stadtman, 1961). The distribution of these enzymes in parasites has been studied by both biochemical and histochemical means (von Brand, 1952; Bullock, 1958; Ma, 1964) and some purification of acid phosphatase has been achieved (Ma, 1964). The objective of the present paper was to determine what phosphomonoesters are attacked by enzymes from Paragonimus kellicotti Ward, 1908, and to what extent. In addition, the enzymes have been partially purified and some of their properties ascertained.

Influence of physical loadings on the histochemical changes in the activity of succinic dehydrogenase, alkaline phosphomonoesterase, and adenosine triphosphatase of the myocardium, liver, and kidneys

Influence of physical loadings on the histochemical changes in the activity of succinic dehydrogenase, alkaline phosphomonoesterase, and adenosine triphosphatase of the myocardium, liver, and kidneys

Alkaline Phosphonionoesterase Activity in Insects. 2. Activity in Various Cell Fractions from the Blow Fly Phormia regina12

The alkaline phosphomonoesterase activity of mitochondrial, microsomal, and soluble fractions prepared from Phormia regina (Meigen) were investigated, and the enzymes were partially purified. The alkaline phosphomonoesterases of these cell fractions are similar in pH optimum, metal ion activation, and stability in the presence and absence of substrate. Minor differences exist in the Michaelis constants, when p -nitrophenyl is used as the substrate, and in their substrate specificity. Manganese and magnesium are the most effective activators of several tested, and, in contrast to the corresponding enzymes in vertebrates, neither copper nor organic sulfhydryl binding agents are effective inhibitors.

ELECTROPHORETIC SEPARATION OF HYDROLYTIC ENZYMES OF THE FEMALE RAT REPRODUCTIVE TRACT.

The nonspecific carboxyl esterases and alkaline and acid phosphomonoesterases were studied in the ovary, oviduct, uterus and vagina of the intact, ovariectomized, salpingectomized or hysterectomized rat by the zymogram method. In the intact animal a single prominent alkaline phosphomonoesterase was evident in each of the reproductive organs. Its activity was greater during the proestrous and estrous periods than during the metestrous or diestrous periods. On occasion, 3 other alkaline phosphomonoesterases were observed in the uterus and vagina. Following ovariectomy, a general decrease in activity of this class of enzymes occurred throughout the genital tract. Conversely, after salpingectomy or hysterectomy, alkaline phosphomonoesterase activity increased in all organs studied. In the intact animal a minimum of 7 esterases in each of the 4 reproductive organs was demonstrated. Four acid phosphomonoesterases were also evident, of which only 2 could be repeatedly reproduced. Although variations in enzyme ac...

Alkaline phosphomonoesterase activity in insects—I. Activity in various enzyme preparations from the blowflies, Phormia regina and Sarcophaga bullata

A relatively non-specific alkaline phosphomonoesterase activity with a pH optimum of approximately 9·3 has been demonstrated in enzyme preparations derived from larvae and adults of the blowflies, Phormia regina and Sarcophaga bullata. The nitrogen-containing phosphate esters, phosphorylcholine, phosphorylethanolamine, and phosphorylserine, as well as other phosphomonoesters, are hydrolysed. Enzyme assays show that the larvae of both species exhibit three to four times the activity of the adults. In both species a shift in the distribution of activity between mitochondria and the S 10.000 fraction can be seen between the larval and adult stages. In the larvae the mitochondria are about twice as active as the S 10.000 fraction while in the adults the S 10.000 fraction is the more active (ca. four times in the case of P. regina and ca. six times in S. bullata). Comparison of the relative rates of hydrolysis of different phosphate esters by different fractions from the same insect indicate that the enzyme or enzyme complex of the mitochondria is different from that of the S 10.000 fraction.

In vitro effects of estradiol on the aorta of chickens.

Aortas of chickens were incubated during 72 hours with 17α- or with 17β-estradiol and the alkaline phosphomonoesterase activity determined. Paired experiments demonstrated that both isomers are able to enhance the activity of the enzyme in vitro. The possible relation of these results with atherogenesis is discussed.

The induction of phosphatase in various organs of the chick embryo

1. 1. Various substrates were injected daily into chick eggs to test their inductive effect on phosphatases in the duodenum, liver, mesonephros, and metanephros of embryos between 14 and 19 days of incubation. 2. 2. Only phenyl phosphate administration significantly increased the activity of alkaline phosphomonoesterase in all organs studied. None of the substrates affected acid phosphomonoesterase activity. Adenosine-5-phosphatase activity was not affected by phenyl phosphate administration. 3. 3. Various observations indicate that the observed increase in alkaline phosphomonoesterase activity is to be taken as an actual synthesis of the enzyme. 4. 4. The patterns of alkaline phosphomonoesterase accumulation following phenyl phosphate administration were analyzed in detail. 5. 5. Histological and histochemical observations show that the induced alkaline phosphomonoesterase has an identical localization with the normal enzyme, and that the induced synthesis of the enzyme is dissociable from morphological differentiation of the organs to a considerable extent. 6. 6. The results obtained were discussed on the basis of the properties and suggested functions of phosphatases from an embryological viewpoint.

Alkaline Phosphatase in Invertebrate Sites of Protein Secretion

Two familiar invertebrates, the caterpillar of the goat-moth (Cossus cossus) and of a common spider (Tegenaria domestica), have been investigated for alkaline phosphomonoesterase activity by the cytochemical technique of Takamatsu1 and of Gomori2,3.